Proteins > Rho-associated protein kinase 1
Page last updated: 2024-08-07 17:05:35
Rho-associated protein kinase 1
A Rho-associated protein kinase 1 that is encoded in the genome of human. [PRO:CNA, UniProtKB:Q13464]
Synonyms
EC 2.7.11.1;
Renal carcinoma antigen NY-REN-35;
Rho-associated, coiled-coil-containing protein kinase 1;
Rho-associated, coiled-coil-containing protein kinase I;
ROCK-I;
p160 ROCK-1;
p160ROCK
Research
Bioassay Publications (47)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 14 (29.79) | 29.6817 |
| 2010's | 26 (55.32) | 24.3611 |
| 2020's | 7 (14.89) | 2.80 |
Compounds (250)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| fasudil | Homo sapiens (human) | Kd | 0.9060 | 1 | 1 |
| 4-(4'-hydroxyphenyl)-amino-6,7-dimethoxyquinazoline | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| imatinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| triciribine phosphate | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| staurosporine | Homo sapiens (human) | Kd | 0.0003 | 1 | 1 |
| picropodophyllin | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| gefitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| lestaurtinib | Homo sapiens (human) | Kd | 10.0373 | 3 | 3 |
| perifosine | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| vatalanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| ruboxistaurin | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| canertinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| birb 796 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| cyc 202 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sb 203580 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| enzastaurin | Homo sapiens (human) | Kd | 23.3333 | 2 | 3 |
| erlotinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| lapatinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| sorafenib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| pd 173955 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| s 1033 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| xl147 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms 387032 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| sf 2370 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tandutinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| vx-745 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| dasatinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| ha 1100 | Homo sapiens (human) | Kd | 0.5320 | 1 | 1 |
| 7-epi-hydroxystaurosporine | Homo sapiens (human) | Kd | 0.9550 | 1 | 1 |
| zd 6474 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| imd 0354 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| alvocidib | Homo sapiens (human) | Kd | 15.6000 | 2 | 2 |
| bosutinib | Homo sapiens (human) | Kd | 15.4350 | 2 | 2 |
| orantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| su 11248 | Homo sapiens (human) | Kd | 10.3067 | 3 | 3 |
| palbociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| vx680 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| cyc 116 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| everolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ekb 569 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| axitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| temsirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pd 184352 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| on 01910 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| av 412 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| telatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| y-39983 | Homo sapiens (human) | EC50 | 0.7900 | 1 | 1 |
| y-39983 | Homo sapiens (human) | Kd | 0.0080 | 1 | 1 |
| cp 547632 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms345541 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| lenvatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pd 0325901 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| midostaurin | Homo sapiens (human) | Kd | 15.2000 | 3 | 3 |
| px-866 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ripasudil | Homo sapiens (human) | Kd | 0.0330 | 1 | 1 |
| osi 930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ki 20227 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| scio-469 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cp 724714 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pi103 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| hmn-214 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tivozanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| hki 272 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| tofacitinib | Homo sapiens (human) | Kd | 1.6000 | 2 | 2 |
| n-(6-chloro-7-methoxy-9h-beta-carbolin-8-yl)-2-methylnicotinamide | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| cediranib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| masitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| ly-2157299 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pazopanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| azd 6244 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| su 14813 | Homo sapiens (human) | Kd | 15.6000 | 2 | 2 |
| bibw 2992 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| binimetinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sotrastaurin | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| aee 788 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| saracatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| vx 702 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| crenolanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tg100-115 | Homo sapiens (human) | Kd | 23.3333 | 2 | 3 |
| cc 401 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms 599626 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| exel-7647 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| volasertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pha 665752 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| azd 7762 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| regorafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| 6-[[5-fluoro-2-(3,4,5-trimethoxyanilino)-4-pyrimidinyl]amino]-2,2-dimethyl-4H-pyrido[3,2-b][1,4]oxazin-3-one | Homo sapiens (human) | Kd | 15.2950 | 2 | 2 |
| brivanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| mp470 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| rgb 286638 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| np 031112 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| at 7519 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| bms-690514 | Homo sapiens (human) | Kd | 2.8160 | 1 | 1 |
| bi 2536 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| inno-406 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| nvp-ast487 | Homo sapiens (human) | Kd | 1.5000 | 1 | 1 |
| kw 2449 | Homo sapiens (human) | Kd | 15.1500 | 2 | 2 |
| danusertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| abt 869 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| azd 8931 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| arq 197 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd 1152 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pf 00299804 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ridaforolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ch 4987655 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| 6-(5-((cyclopropylamino)carbonyl)-3-fluoro-2-methylphenyl)-n-(2,2-dimethylprpyl)-3-pyridinecarboxamide | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cortistatin a | Homo sapiens (human) | Kd | 0.2500 | 1 | 1 |
| cc-930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gw 2580 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| tak 285 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| idelalisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| crizotinib | Homo sapiens (human) | Kd | 16.8500 | 2 | 2 |
| osi 906 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| chir-265 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| motesanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| fostamatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| trametinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mln8054 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| pf-562,271 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| GDC-0879 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| jnj-26483327 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ly2603618 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tg100801 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| dactolisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| bgt226 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 461364 | Homo sapiens (human) | Kd | 17.4500 | 2 | 2 |
| azd 1152-hqpa | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| nvp-tae684 | Homo sapiens (human) | Kd | 0.0370 | 1 | 1 |
| enmd 2076 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| e 7050 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| 2-amino-8-ethyl-4-methyl-6-(1H-pyrazol-5-yl)-7-pyrido[2,3-d]pyrimidinone | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tak-901 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gdc-0973 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| buparlisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd 1480 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd8330 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pha 848125 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ro5126766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| fedratinib | Homo sapiens (human) | Kd | 20.7000 | 2 | 3 |
| gsk690693 | Homo sapiens (human) | Kd | 1.4780 | 2 | 2 |
| 14-methyl-20-oxa-5,7,14,26-tetraazatetracyclo(19.3.1.1(2,6).1(8,12))heptacosa-1(25),2(26),3,5,8(27),9,11,16,21,23-decaene | Homo sapiens (human) | Kd | 99.2330 | 1 | 1 |
| azd5438 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pf 04217903 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gdc 0941 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| icotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ph 797804 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| kx-01 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| plx 4720 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| mk 5108 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cx 4945 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cudc 101 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| arry-614 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tak 593 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mln 8237 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sgx 523 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| bms 754807 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms 777607 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sgi 1776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pci 32765 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ponatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| amg 900 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk-1775 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| AMG-208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| quizartinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| at13148 | Homo sapiens (human) | Kd | 0.0270 | 1 | 1 |
| tak 733 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| mk 2206 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sns 314 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| lucitanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pf-04691502 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| n-(cyanomethyl)-4-(2-((4-(4-morpholinyl)phenyl)amino)-4-pyrimidinyl)benzamide | Homo sapiens (human) | Kd | 1.3620 | 1 | 1 |
| dcc-2036 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cabozantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| defactinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ly2584702 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| incb-018424 | Homo sapiens (human) | Kd | 0.4395 | 2 | 2 |
| poziotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| asp3026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| entrectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pexidartinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| TAK-580 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 2126458 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| emd1214063 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 1838705a | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| pf 3758309 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gdc 0980 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd2014 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| (5-(2,4-bis((3s)-3-methylmorpholin-4-yl)pyrido(2,3-d)pyrimidin-7-yl)-2-methoxyphenyl)methanol | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| plx4032 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk 1363089 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| arry-334543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| kin-193 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk 2461 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bay 869766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| as 703026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| baricitinib | Homo sapiens (human) | Kd | 0.4820 | 1 | 1 |
| dabrafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pki 587 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| n-(3-fluoro-4-((1-methyl-6-(1h-pyrazol-4-yl)-1h-indazol-5 yl)oxy)phenyl)-1-(4-fluorophenyl)-6-methyl-2-oxo-1,2-dihydropyridine-3-carboxamide | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ribociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk-8033 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pha 793887 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sb 1518 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| abemaciclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk-8776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| afuresertib | Homo sapiens (human) | Kd | 2.1440 | 1 | 1 |
| gsk 1070916 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| jnj38877605 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| dinaciclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gilteritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| alectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| glpg0634 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| encorafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms-911543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gsk2141795 | Homo sapiens (human) | Kd | 1.1520 | 1 | 1 |
| azd8186 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| byl719 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cep-32496 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| rociletinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ceritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| azd1208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| vx-509 | Homo sapiens (human) | Kd | 13.4620 | 1 | 1 |
| debio 1347 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| volitinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| osimertinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| at 9283 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| otssp167 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| chir 258 | Homo sapiens (human) | Kd | 15.3800 | 2 | 2 |
| osi 027 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| nintedanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| bay 80-6946 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pp242 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
Identification of 5H-chromeno[3,4-c]pyridine and 6H-isochromeno[3,4-c]pyridine derivatives as potent and selective dual ROCK inhibitors.Bioorganic & medicinal chemistry letters, , 11-01, Volume: 30, Issue:21, 2020
Ocular Disease Therapeutics: Design and Delivery of Drugs for Diseases of the Eye.Journal of medicinal chemistry, , 10-08, Volume: 63, Issue:19, 2020
Potently inhibiting cancer cell migration with novel 3H-pyrazolo[4,3-f]quinoline boronic acid ROCK inhibitors.European journal of medicinal chemistry, , Oct-15, Volume: 180, 2019
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of Molecular Therapeutics for Glaucoma: Challenges, Successes, and Promising Directions.Journal of medicinal chemistry, , Feb-11, Volume: 59, Issue:3, 2016
Design, Synthesis, and Structure-Activity Relationships of Pyridine-Based Rho Kinase (ROCK) Inhibitors.Journal of medicinal chemistry, , Jun-25, Volume: 58, Issue:12, 2015
Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2).MedChemComm, , Jun-01, Volume: 3, Issue:6, 2012
Fragment-based discovery of 6-substituted isoquinolin-1-amine based ROCK-I inhibitors.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 21, Issue:1, 2011
Substituted 2H-isoquinolin-1-one as potent Rho-Kinase inhibitors. Part 1: Hit-to-lead account.Bioorganic & medicinal chemistry letters, , Jun-01, Volume: 20, Issue:11, 2010
Hit to lead account of the discovery of bisbenzamide and related ureidobenzamide inhibitors of Rho kinase.Journal of medicinal chemistry, , Jan-28, Volume: 53, Issue:2, 2010
Design and synthesis of rho kinase inhibitors (III).Bioorganic & medicinal chemistry, , Jan-15, Volume: 15, Issue:2, 2007
Novel Rho kinase inhibitors with anti-inflammatory and vasodilatory activities.The Journal of pharmacology and experimental therapeutics, , Volume: 320, Issue:1, 2007
The structure of dimeric ROCK I reveals the mechanism for ligand selectivity.The Journal of biological chemistry, , Jan-06, Volume: 281, Issue:1, 2006
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
ASR352, A potent anticancer agent: Synthesis, preliminary SAR, and biological activities against colorectal cancer bulk, 5-fluorouracil/oxaliplatin resistant and stem cells.European journal of medicinal chemistry, , Jan-01, Volume: 161, 2019
Novel quinazoline derivatives bearing various 6-benzamide moieties as highly selective and potent EGFR inhibitors.Bioorganic & medicinal chemistry, , 05-01, Volume: 26, Issue:8, 2018
Novel LCK/FMS inhibitors based on phenoxypyrimidine scaffold as potential treatment for inflammatory disorders.European journal of medicinal chemistry, , Dec-01, Volume: 141, 2017
Design, synthesis and biological evaluation of pyrazol-furan carboxamide analogues as novel Akt kinase inhibitors.European journal of medicinal chemistry, , Jul-19, Volume: 117, 2016
Investigation of new 2-aryl substituted Benzothiopyrano[4,3-d]pyrimidines as kinase inhibitors targeting vascular endothelial growth factor receptor 2.European journal of medicinal chemistry, , Oct-20, Volume: 103, 2015
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Synthesis, activity, and pharmacophore development for isatin-beta-thiosemicarbazones with selective activity toward multidrug-resistant cells.Journal of medicinal chemistry, , May-28, Volume: 52, Issue:10, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragment-based drug design (vFBDD).Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 21, Issue:23, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
Design, Synthesis, and Structure-Activity Relationships of Pyridine-Based Rho Kinase (ROCK) Inhibitors.Journal of medicinal chemistry, , Jun-25, Volume: 58, Issue:12, 2015
Novel ROCK inhibitors for the treatment of pulmonary arterial hypertension.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 24, Issue:20, 2014
Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2).MedChemComm, , Jun-01, Volume: 3, Issue:6, 2012
Fragment-based discovery of 6-substituted isoquinolin-1-amine based ROCK-I inhibitors.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 21, Issue:1, 2011
Hit to lead account of the discovery of bisbenzamide and related ureidobenzamide inhibitors of Rho kinase.Journal of medicinal chemistry, , Jan-28, Volume: 53, Issue:2, 2010
Novel Rho kinase inhibitors with anti-inflammatory and vasodilatory activities.The Journal of pharmacology and experimental therapeutics, , Volume: 320, Issue:1, 2007
The structure of dimeric ROCK I reveals the mechanism for ligand selectivity.The Journal of biological chemistry, , Jan-06, Volume: 281, Issue:1, 2006
Novel ROCK inhibitors for the treatment of pulmonary arterial hypertension.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 24, Issue:20, 2014
Hit to lead account of the discovery of bisbenzamide and related ureidobenzamide inhibitors of Rho kinase.Journal of medicinal chemistry, , Jan-28, Volume: 53, Issue:2, 2010
The structure of dimeric ROCK I reveals the mechanism for ligand selectivity.The Journal of biological chemistry, , Jan-06, Volume: 281, Issue:1, 2006
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
The Discovery of VX-745: A Novel and Selective p38α Kinase Inhibitor.ACS medicinal chemistry letters, , Oct-13, Volume: 2, Issue:10, 2011
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Dual-target inhibitors of poly (ADP-ribose) polymerase-1 for cancer therapy: Advances, challenges, and opportunities.European journal of medicinal chemistry, , Feb-15, Volume: 230, 2022
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Design, Synthesis, and Structure-Activity Relationships of Pyridine-Based Rho Kinase (ROCK) Inhibitors.Journal of medicinal chemistry, , Jun-25, Volume: 58, Issue:12, 2015
Fragment-based discovery of 6-substituted isoquinolin-1-amine based ROCK-I inhibitors.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 21, Issue:1, 2011
Hit to lead account of the discovery of bisbenzamide and related ureidobenzamide inhibitors of Rho kinase.Journal of medicinal chemistry, , Jan-28, Volume: 53, Issue:2, 2010
The structure of dimeric ROCK I reveals the mechanism for ligand selectivity.The Journal of biological chemistry, , Jan-06, Volume: 281, Issue:1, 2006
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
In vivo optimization of 2,3-diaminopyrazine Rho Kinase inhibitors for the treatment of glaucoma.Bioorganic & medicinal chemistry letters, , Apr-15, Volume: 24, Issue:8, 2014
Benzothiophene containing Rho kinase inhibitors: Efficacy in an animal model of glaucoma.Bioorganic & medicinal chemistry letters, , Jun-01, Volume: 20, Issue:11, 2010
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
Identification of 5H-chromeno[3,4-c]pyridine and 6H-isochromeno[3,4-c]pyridine derivatives as potent and selective dual ROCK inhibitors.Bioorganic & medicinal chemistry letters, , 11-01, Volume: 30, Issue:21, 2020
Ocular Disease Therapeutics: Design and Delivery of Drugs for Diseases of the Eye.Journal of medicinal chemistry, , 10-08, Volume: 63, Issue:19, 2020
p62/SQSTM1, a Central but Unexploited Target: Advances in Its Physiological/Pathogenic Functions and Small Molecular Modulators.Journal of medicinal chemistry, , 09-24, Volume: 63, Issue:18, 2020
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of Molecular Therapeutics for Glaucoma: Challenges, Successes, and Promising Directions.Journal of medicinal chemistry, , Feb-11, Volume: 59, Issue:3, 2016
Identification of 5H-chromeno[3,4-c]pyridine and 6H-isochromeno[3,4-c]pyridine derivatives as potent and selective dual ROCK inhibitors.Bioorganic & medicinal chemistry letters, , 11-01, Volume: 30, Issue:21, 2020
Substituted 2H-isoquinolin-1-one as potent Rho-Kinase inhibitors. Part 1: Hit-to-lead account.Bioorganic & medicinal chemistry letters, , Jun-01, Volume: 20, Issue:11, 2010
A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases.Proceedings of the National Academy of Sciences of the United States of America, , Dec-18, Volume: 104, Issue:51, 2007
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of 3-(1H-indol-3-yl)-4-[2-(4-methylpiperazin-1-yl)quinazolin-4-yl]pyrrole-2,5-dione (AEB071), a potent and selective inhibitor of protein kinase C isotypes.Journal of medicinal chemistry, , Oct-22, Volume: 52, Issue:20, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Identification of 4-(2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-{[(3S)-3-piperidinylmethyl]oxy}-1H-imidazo[4,5-c]pyridin-4-yl)-2-methyl-3-butyn-2-ol (GSK690693), a novel inhibitor of AKT kinase.Journal of medicinal chemistry, , Sep-25, Volume: 51, Issue:18, 2008
(1H-imidazo[4,5-c]pyridin-2-yl)-1,2,5-oxadiazol-3-ylamine derivatives: further optimisation as highly potent and selective MSK-1-inhibitors.Bioorganic & medicinal chemistry letters, , Jul-15, Volume: 15, Issue:14, 2005
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Potently inhibiting cancer cell migration with novel 3H-pyrazolo[4,3-f]quinoline boronic acid ROCK inhibitors.European journal of medicinal chemistry, , Oct-15, Volume: 180, 2019
Discovery of aminofurazan-azabenzimidazoles as inhibitors of Rho-kinase with high kinase selectivity and antihypertensive activity.Journal of medicinal chemistry, , Jan-11, Volume: 50, Issue:1, 2007
Novel Rho kinase inhibitors with anti-inflammatory and vasodilatory activities.The Journal of pharmacology and experimental therapeutics, , Volume: 320, Issue:1, 2007
Potently inhibiting cancer cell migration with novel 3H-pyrazolo[4,3-f]quinoline boronic acid ROCK inhibitors.European journal of medicinal chemistry, , Oct-15, Volume: 180, 2019
Novel ROCK inhibitors for the treatment of pulmonary arterial hypertension.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 24, Issue:20, 2014
Novel Rho kinase inhibitors with anti-inflammatory and vasodilatory activities.The Journal of pharmacology and experimental therapeutics, , Volume: 320, Issue:1, 2007
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Identification of 4-(2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-{[(3S)-3-piperidinylmethyl]oxy}-1H-imidazo[4,5-c]pyridin-4-yl)-2-methyl-3-butyn-2-ol (GSK690693), a novel inhibitor of AKT kinase.Journal of medicinal chemistry, , Sep-25, Volume: 51, Issue:18, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Discovery of 3,4,6-Trisubstituted Piperidine Derivatives as Orally Active, Low hERG Blocking Akt Inhibitors via Conformational Restriction and Structure-Based Design.Journal of medicinal chemistry, , 08-08, Volume: 62, Issue:15, 2019
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Medulloblastoma drugs in development: Current leads, trials and drawbacks.European journal of medicinal chemistry, , Apr-05, Volume: 215, 2021
Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2).MedChemComm, , Jun-01, Volume: 3, Issue:6, 2012
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Enables
This protein enables 10 target(s):
| Target | Category | Definition |
|---|
| protein kinase activity | molecular function | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. [PMID:25399640] |
| protein serine/threonine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. [GOC:bf, MetaCyc:PROTEIN-KINASE-RXN, PMID:2956925] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| ATP binding | molecular function | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732] |
| small GTPase binding | molecular function | Binding to a small monomeric GTPase. [GOC:mah, PMID:27218782] |
| metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
| tau protein binding | molecular function | Binding to tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS. [GOC:jid] |
| tau-protein kinase activity | molecular function | Catalysis of the reaction: ATP + tau-protein = ADP + O-phospho-tau-protein. [EC:2.7.11.26, MetaCyc:TAU-PROTEIN-KINASE-RXN] |
| Rho-dependent protein serine/threonine kinase activity | molecular function | Rho GTPase-dependent catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. [GOC:ecd, PMID:12778124, PMID:20230755] |
| protein serine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989] |
Located In
This protein is located in 12 target(s):
| Target | Category | Definition |
|---|
| Golgi membrane | cellular component | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. [GOC:mah] |
| ruffle | cellular component | Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. [ISBN:0124325653] |
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| centriole | cellular component | A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle. [ISBN:0198547684] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
| cytoskeleton | cellular component | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. [GOC:mah, PMID:16959967, PMID:27419875] |
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
| cytoplasmic stress granule | cellular component | A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. [GOC:ans, PMID:17284590, PMID:17601829, PMID:17967451, PMID:20368989] |
| lamellipodium | cellular component | A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments. [ISBN:0815316194] |
| bleb | cellular component | A cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Blebs are formed during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses. [GOC:mtg_apoptosis, PMID:12083798, PMID:16624291, Wikipedia:Bleb_(cell_biology)] |
| secretory granule lumen | cellular component | The volume enclosed by the membrane of a secretory granule. [GOC:rph] |
| Schaffer collateral - CA1 synapse | cellular component | A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell. [PMID:16399689] |
Active In
This protein is active in 3 target(s):
| Target | Category | Definition |
|---|
| cytoskeleton | cellular component | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. [GOC:mah, PMID:16959967, PMID:27419875] |
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
| cytoplasmic stress granule | cellular component | A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. [GOC:ans, PMID:17284590, PMID:17601829, PMID:17967451, PMID:20368989] |
Involved In
This protein is involved in 64 target(s):
| Target | Category | Definition |
|---|
| epithelial to mesenchymal transition | biological process | A transition where an epithelial cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell. [GOC:dph, PMID:14701881] |
| aortic valve morphogenesis | biological process | The process in which the structure of the aortic valve is generated and organized. [GOC:mtg_heart] |
| apical constriction | biological process | The actin-mediated process that results in the contraction of the apical end of a polarized columnar epithelial cell. [GOC:ascb_2009, GOC:dph, GOC:tb] |
| protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |
| smooth muscle contraction | biological process | A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. [GOC:ef, GOC:jl, GOC:mtg_muscle, ISBN:0198506732] |
| leukocyte cell-cell adhesion | biological process | The attachment of a leukocyte to another cell via adhesion molecules. [GOC:go_curators] |
| signal transduction | biological process | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. [GOC:go_curators, GOC:mtg_signaling_feb11] |
| canonical NF-kappaB signal transduction | biological process | An intracellular signaling cassette characterized by the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB, also known as the canonical NF-kappaB signaling cascade. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. The canonical NF-kappaB pathway is mainly stimulated by proinflammatory cytokines such as IL-1beta, tumor necrosis factor (TNF)-alpha, antigen ligands, and toll-like receptors (TLRs). [GOC:bf, PMID:12773372, PMID:34659217] |
| Rho protein signal transduction | biological process | An intracellular signaling cassette in which a small monomeric GTPase of the Rho subfamily relays a signal. [GOC:bf] |
| positive regulation of autophagy | biological process | Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. [GOC:dph, GOC:tb] |
| positive regulation of cardiac muscle hypertrophy | biological process | Any process that increases the rate, frequency or extent of the enlargement or overgrowth of all or part of the heart due to an increase in size (not length) of individual cardiac muscle fibers, without cell division. [GOC:BHF, GOC:dph, GOC:tb] |
| positive regulation of gene expression | biological process | Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). [GOC:txnOH-2018] |
| positive regulation of phosphatase activity | biological process | Any process that increases the rate or frequency of phosphatase activity. Phosphatases catalyze the hydrolysis of phosphoric monoesters, releasing inorganic phosphate. [GOC:BHF, GOC:dph, GOC:tb] |
| negative regulation of angiogenesis | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of angiogenesis. [GOC:go_curators] |
| peptidyl-serine phosphorylation | biological process | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037] |
| membrane to membrane docking | biological process | The initial attachment of a membrane to a target membrane, mediated by proteins protruding from the two membranes. Docking requires only that the membranes come close enough for the proteins to interact and adhere. [GOC:isa_complete] |
| actin cytoskeleton organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. [GOC:dph, GOC:jl, GOC:mah] |
| regulation of cell adhesion | biological process | Any process that modulates the frequency, rate or extent of attachment of a cell to another cell or to the extracellular matrix. [GOC:mah] |
| regulation of cell migration | biological process | Any process that modulates the frequency, rate or extent of cell migration. [GOC:go_curators] |
| cortical actin cytoskeleton organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane. [GOC:dph, GOC:jl, GOC:mah, GOC:pf] |
| neuron projection development | biological process | The process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites). [GOC:mah] |
| bleb assembly | biological process | The assembly of a bleb, a cell extension caused by localized decoupling of the cytoskeleton from the plasma membrane and characterized by rapid formation, rounded shape, and scarcity of organelles within the protrusion. Plasma membrane blebbing occurs during apoptosis and other cellular processes, including cell locomotion, cell division, and as a result of physical or chemical stresses. [GOC:mah, GOC:mtg_apoptosis, PMID:12083798, PMID:16624291, Wikipedia:Bleb_(cell_biology)] |
| negative regulation of protein binding | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding. [GOC:mah] |
| regulation of actin cytoskeleton organization | biological process | Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. [GOC:mah] |
| positive regulation of dephosphorylation | biological process | Any process that activates or increases the frequency, rate or extent of removal of phosphate groups from a molecule. [GOC:bf] |
| negative regulation of myosin-light-chain-phosphatase activity | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of myosin-light-chain-phosphatase activity. [GOC:bf, GOC:go_curators] |
| negative regulation of phosphorylation | biological process | Any process that stops, prevents or decreases the rate of addition of phosphate groups to a molecule. [GOC:jl] |
| positive regulation of MAPK cascade | biological process | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade. [GOC:go_curators] |
| regulation of keratinocyte differentiation | biological process | Any process that modulates the frequency, rate or extent of keratinocyte differentiation. [GOC:go_curators] |
| regulation of neuron differentiation | biological process | Any process that modulates the frequency, rate or extent of neuron differentiation. [GOC:go_curators] |
| leukocyte migration | biological process | The movement of a leukocyte within or between different tissues and organs of the body. [GOC:add, ISBN:0781735149, PMID:14680625, PMID:14708592, PMID:7507411, PMID:8600538] |
| leukocyte tethering or rolling | biological process | Transient adhesive interactions between leukocytes and endothelial cells lining blood vessels. Carbohydrates on circulating leukocytes bind selectins on the vessel wall causing the leukocytes to slow down and roll along the inner surface of the vessel wall. During this rolling motion, transitory bonds are formed and broken between selectins and their ligands. Typically the first step in cellular extravasation (the movement of leukocytes out of the circulatory system, towards the site of tissue damage or infection). [GOC:bf, ISBN:0781735149, PMID:14680625, PMID:14708592, PMID:7507411, PMID:8600538, Wikipedia:Leukocyte_extravasation] |
| negative regulation of membrane protein ectodomain proteolysis | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of membrane protein ectodomain proteolysis. [GOC:ai] |
| myoblast migration | biological process | The orderly movement of a myoblast from one site to another, often during the development of a multicellular organism. A myoblast is a cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers. [CL:0000056, GOC:ai, GOC:mtg_muscle] |
| regulation of stress fiber assembly | biological process | Any process that modulates the frequency, rate or extent of the assembly of a stress fiber, a bundle of microfilaments and other proteins found in fibroblasts. [GOC:ai] |
| regulation of focal adhesion assembly | biological process | Any process that modulates the frequency, rate or extent of focal adhesion formation, the establishment and maturation of focal adhesions. [GOC:ai] |
| positive regulation of focal adhesion assembly | biological process | Any process that activates or increases the frequency, rate or extent of focal adhesion assembly, the establishment and maturation of focal adhesions. [GOC:ai] |
| mRNA destabilization | biological process | Any process that decreases the stability of an mRNA molecule, making it more vulnerable to degradative processes. Messenger RNA is the intermediate molecule between DNA and protein. It includes UTR and coding sequences. It does not contain introns. [GOC:dph, GOC:jh] |
| negative regulation of biomineral tissue development | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of biomineral tissue development, the formation of hard tissues that consist mainly of inorganic compounds. [GOC:mah] |
| regulation of microtubule cytoskeleton organization | biological process | Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins. [GOC:mah] |
| response to transforming growth factor beta | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a transforming growth factor beta stimulus. [GOC:mah] |
| protein localization to plasma membrane | biological process | A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane. [GOC:mah] |
| regulation of synapse maturation | biological process | Any process that modulates the extent of synapse maturation, the process that organizes a synapse so that it attains its fully functional state. [GOC:ascb_2009, GOC:dph, GOC:tb] |
| podocyte cell migration | biological process | The orderly movement of a podocyte from one site to another, often during the development of a multicellular organism or multicellular structure. A podocyte is a specialized kidney epithelial cell. [GOC:pm, PMID:21402783] |
| motor neuron apoptotic process | biological process | Any apoptotic process in a motor neuron, an efferent neuron that passes from the central nervous system or a ganglion toward or to a muscle and conducts an impulse that causes movement. [CL:0000100, GOC:BHF, GOC:mtg_apoptosis, PMID:14523086] |
| blood vessel diameter maintenance | biological process | Any process that modulates the diameter of blood vessels. [GOC:pr] |
| regulation of angiotensin-activated signaling pathway | biological process | Any process that modulates the frequency, rate or extent of the angiotensin-activated signaling pathway. [GOC:lf, PMID:28784619] |
| neuron projection arborization | biological process | The process in which the anatomical structures of a neuron projection are generated and organized into branches. A neuron projection is any process extending from a neural cell, such as axons or dendrites. [GOC:aruk, GOC:bc, PMID:17114044, PMID:23270857, PMID:23764288] |
| positive regulation of amyloid-beta clearance | biological process | Any process that activates or increases the frequency, rate or extent of amyloid-beta clearance. [GOC:BHF, GOC:TermGenie] |
| regulation of synaptic vesicle endocytosis | biological process | Any process that modulates the frequency, rate or extent of synaptic vesicle endocytosis. [GOC:BHF, GOC:TermGenie] |
| negative regulation of amyloid-beta formation | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of amyloid-beta formation. [GOC:hjd, GOC:TermGenie, PMID:22992957] |
| negative regulation of amyloid precursor protein catabolic process | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of amyloid precursor protein catabolic process. [GO_REF:0000058, GOC:PARL, GOC:rl, GOC:TermGenie, PMID:24499793] |
| regulation of establishment of endothelial barrier | biological process | Any process that modulates the frequency, rate or extent of establishment of endothelial barrier. [GO_REF:0000058, GOC:als, GOC:TermGenie, PMID:24851274] |
| negative regulation of bicellular tight junction assembly | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of tight junction assembly. [GO_REF:0000058, GOC:jz, GOC:TermGenie, PMID:25050009] |
| positive regulation of connective tissue replacement | biological process | Any process that activates or increases the frequency, rate or extent of connective tissue replacement. [GO_REF:0000058, GOC:bc, GOC:BHF, GOC:BHF_miRNA, GOC:TermGenie, PMID:25590961] |
| response to angiotensin | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an angiotensin stimulus. Angiotensin is any of three physiologically active peptides (angiotensin II, III, or IV) processed from angiotensinogen. [PMID:22982863] |
| regulation of establishment of cell polarity | biological process | Any process that modulates the frequency, rate or extent of establishment of cell polarity. [GOC:dph] |
| regulation of cell motility | biological process | Any process that modulates the frequency, rate or extent of cell motility. [GOC:mah] |
| negative regulation of motor neuron apoptotic process | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of motor neuron apoptotic process. [GOC:mtg_apoptosis, GOC:obol] |
| regulation of cell junction assembly | biological process | Any process that modulates the frequency, rate or extent of cell junction assembly. [GOC:TermGenie] |
| mitotic cytokinesis | biological process | A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells. [GOC:mtg_cell_cycle] |
| embryonic morphogenesis | biological process | The process in which anatomical structures are generated and organized during the embryonic phase. The embryonic phase begins with zygote formation. The end of the embryonic phase is organism-specific. For example, it would be at birth for mammals, larval hatching for insects and seed dormancy in plants. [GOC:jid, GOC:mtg_sensu] |
| peptidyl-threonine phosphorylation | biological process | The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. [RESID:AA0038] |
| actomyosin structure organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin. The myosin may be organized into filaments. [GOC:dph, GOC:jl, GOC:mah] |